Reversible membrane association of heat-shock protein 22 in Chlamydomonas reinhardtii during heat shock and recovery.

The process of reversible membrane association of the nuclear-encoded heat-shock protein hsp22 in Chlamydomonas reinhardtii cells during recovery from heat stress has been investigated. hsp22 associates with a chloroplast membrane-enriched fraction, dissociates from the membranes during recovery from heat shock and rebinds during a subsequent heat-shock treatment in vivo. The protein remains in the cell soluble fraction for at least 22 h after heat-stress treatment. Dissociation of membrane-bound hsp22 occurs only at 25-38 degrees C and reassociation occurs only at the hsp22 induction temperature (38-42 degrees C). Hsp22 dissociation from the membrane fraction is not related to de novo protein synthesis in vivo and does not occur in vitro. Based on the derived amino acid sequence, hsp22 is not considered a typical chloroplast-associated heat-shock protein [Vierling, E. (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol. 42, 579-620] and may be associated with the chloroplast envelope membrane. However, the reversible association of hsp22 with the chloroplast-enriched membrane fraction indicates similar properties to those of pea low-molecular-mass heat-shock proteins [Glaczinski, H. & Kloppstech, K. (1988) Eur. J. Biochem. 173, 579-583] and may be related to the transient response of the chloroplast to heat stress.